Orientation difference of chemically immobilized and physically adsorbed biological molecules on polymers detected at the solid/liquid interfaces in situ

Ye, Shuji, Nguyen, Khoi Tan, Boughton, Andrew P., Mello, Charlene M. and Chen, Zhan (2010) Orientation difference of chemically immobilized and physically adsorbed biological molecules on polymers detected at the solid/liquid interfaces in situ. Langmuir, 26 9: 6471-6477. doi:10.1021/la903932w


Author Ye, Shuji
Nguyen, Khoi Tan
Boughton, Andrew P.
Mello, Charlene M.
Chen, Zhan
Title Orientation difference of chemically immobilized and physically adsorbed biological molecules on polymers detected at the solid/liquid interfaces in situ
Journal name Langmuir   Check publisher's open access policy
ISSN 0743-7463
1520-5827
Publication date 2010-05-04
Year available 2010
Sub-type Article (original research)
DOI 10.1021/la903932w
Volume 26
Issue 9
Start page 6471
End page 6477
Total pages 7
Place of publication Washington, DC United States
Publisher American Chemical Society
Collection year 2010
Language eng
Subject 1603 Demography
3104 Condensed Matter Physics
3110 Surfaces and Interfaces
2500 Materials Science
1607 Social Work
Abstract A surface sensitive second order nonlinear optical technique, sum frequency generation vibrational spectroscopy, was applied to study peptide orientation on polymer surfaces, supplemented by a linear vibrational spectroscopy, attenuated total reflectance Fourier transform infrared spectroscopy. Using the antimicrobial peptide Cecropin P1 as a model system, we have quantitatively demonstrated that chemically immobilized peptides on polymers adopt a more ordered orientation than less tightly bound physically adsorbed peptides. These differences were also observed in different chemical environments, for example, air versus water. Although numerous studies have reported a direct correlation between the choice of immobilization method and the performance of an attached biological molecule, the lack of direct biomolecular structure and orientation data has made it difficult to elucidate the relationship between structure, orientation, and function at a surface. In this work, we directly studied the effect of chemical immobilization method on biomolecular orientation/ordering, an important step for future studies of biomolecular activity. The methods for orientation analysis described within are also of relevance to understanding biosensors, biocompatibility, marine-antifouling, membrane protein functions, and antimicrobial peptide activities.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemical Engineering Publications
 
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